Hao Huilin, Eberand Benjamin M, Larance Mark, Haltiwanger Robert S
Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30605, USA.
Charles Perkins Centre, School of Medical Sciences, Faculty of Medicine and Health, The University of Sydney, Sydney, NSW 2006, Australia.
Molecules. 2025 Mar 26;30(7):1470. doi: 10.3390/molecules30071470.
Domain-specific -fucosylation is an unusual type of glycosylation, where the fucose is directly attached to the serine or threonine residues in specific protein domains via an -linkage. -fucosylated proteins play critical roles in a wide variety of biological events and hold important therapeutic values, with the most studied being the Notch receptors and ADAMTS proteins. -fucose glycans modulate the function of the proteins they modify and are closely associated with various diseases including cancer. In mammals, alongside the well-documented protein -fucosyltransferase (POFUT) 1-mediated -fucosylation of epidermal growth factor-like (EGF) repeats and POFUT2-mediated -fucosylation of thrombospondin type 1 repeats (TSRs), a new type of -fucosylation was recently identified on elastin microfibril interface (EMI) domains, mediated by POFUT3 and POFUT4 (formerly FUT10 and FUT11). In this review, we present an overview of our current knowledge of -fucosylation, integrating the latest findings and with a particular focus on its biological functions and molecular mechanisms.
结构域特异性岩藻糖基化是一种不寻常的糖基化类型，其中岩藻糖通过α-连接直接连接到特定蛋白质结构域中的丝氨酸或苏氨酸残基上。α-岩藻糖基化蛋白在多种生物学事件中发挥关键作用，并具有重要的治疗价值，其中研究最多的是Notch受体和ADAMTS蛋白。α-岩藻糖聚糖调节它们所修饰蛋白质的功能，并与包括癌症在内的各种疾病密切相关。在哺乳动物中，除了有充分文献记载的蛋白质α-岩藻糖基转移酶（POFUT）1介导的表皮生长因子样（EGF）重复序列的α-岩藻糖基化和POFUT2介导的血小板反应蛋白1型重复序列（TSR）的α-岩藻糖基化外，最近还在弹性蛋白微原纤维界面（EMI）结构域上发现了一种新型的α-岩藻糖基化，由POFUT3和POFUT4（以前称为FUT10和FUT11）介导。在这篇综述中，我们概述了目前对α-岩藻糖基化的认识，整合了最新的研究结果，并特别关注其生物学功能和分子机制。
